Dr. Richard J Auchus MD
Endocrinology-Diabetes | Endocrinology, Diabetes & Metabolism
5323 Harry Hines Blvd Dallas TX, 75390About
Dr. Richard Auchus is a professor of Internal Medicine, Division of Metabolism, Endocrinology & Diabetes (MEND) and director of the MEND Fellowship Program. He received his medical degree and Ph.D. in ...
Education and Training
Washington Univ Sch Of Med- St Louis Mo 1988
Washington University in St. Louis School of Medicine 1988
Provider Details
Expert Publications
Data provided by the National Library of Medicine- Medroxyprogesterone acetate and dexamethasone are competitive inhibitors of different human steroidogenic enzymes.
- Molecular modeling of human P450c17 (17alpha-hydroxylase/17,20-lyase): insights into reaction mechanisms and effects of mutations.
- Estrogen: consequences and implications of human mutations in synthesis and action.
- Role of cytochrome b5 in the 17,20-lyase activity of P450c17.
- Enzymatic activities of P450c17 stably expressed in fibroblasts from patients with the polycystic ovary syndrome.
- Molecular modeling of the hamster adrenal P450C17.
- Thiazolidinediones but not metformin directly inhibit the steroidogenic enzymes P450c17 and 3beta -hydroxysteroid dehydrogenase.
- The genetics, pathophysiology, and management of human deficiencies of P450c17.
- Pitfalls in characterizing P450c17 mutations associated with isolated 17,20-lyase deficiency.
- Evidence that androgens are the primary steroids produced by Xenopus laevis ovaries and may signal through the classical androgen receptor to promote oocyte maturation.
- Comparison of the hamster and human adrenal P450c17 (17 alpha-hydroxylase/17,20-lyase) using site-directed mutagenesis and molecular modeling.
- Molecular evolution of adrenarche: structural and functional analysis of p450c17 from four primate species.
- Towards a unifying mechanism for CYP17 mutations that cause isolated 17,20-lyase deficiency.
- Molecular dynamics of substrate complexes with hamster cytochrome P450c17 (CYP17): mechanistic approach to understanding substrate binding and activities.
- Aldo is back: recent advances and unresolved controversies in hyperaldosteronism.
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